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Biochemistry (Mosc) ; 72(1): 21-8, 2007 Jan.
Article in English | MEDLINE | ID: mdl-17309433

ABSTRACT

Substrate specificity of Escherichia coli thymidine phosphorylase to thymidine derivatives modified at 5' -, 3' -, and 2' ,3' - positions of the sugar moiety was studied. Equilibrium and kinetic constants (K(m), K(I), k(cat)) of the phosphorolysis reaction have been determined for 20 thymidine analogs. The results are compared with X-ray and molecular dynamics data. The most important hydrogen bonds in the enzyme-substrate complex are revealed.


Subject(s)
Amino Acid Substitution , Escherichia coli/enzymology , Thymidine Phosphorylase/chemistry , Thymidine/metabolism , Catalytic Domain , Crystallography, X-Ray , Hydrogen-Ion Concentration , Molecular Structure , Nucleosides/metabolism , Structure-Activity Relationship , Substrate Specificity , Thymidine Phosphorylase/metabolism
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